text: An illustration of the MSIA procedure is depicted in the figure to the right. Analytes in a biological liquid sample are collected from solution by using a MSIA tip (also known as MSIA microcolumns) that contains a derivatized affinity frit.  Biological samples contain various proteins that span a wide dynamic range so purification is needed to minimize the complex matrix and maximize mass spectrometry sensitivity. the MSIA tip serves as a place to purify these samples by immobilizing the analyte with high selectivity and specificity. Analytes are bound to the frit based on their affinities and all other nonspecific molecules are rinsed away. The specific targets are then eluted on to a mass spectrometer target plate with a MALDI matrix. However, proteins may be digested prior to ms analysis. A MALDI-TOF-MS later follows and targeted analytes are detected based on their m/z values. This method is qualitative, but  the addition of mass shifted variants of the analyte for use as an internal standard makes this method useful for quantitative analysis.
  Pipetor tips, which have been termed MSIA tips or affinity pipette tips play a key role in the process of detecting analytes within biological samples. MSIA tips typically contain porous solid support which has derivatized antigens or antibodies covalently attached. Different analytes have different affinity for the tips so it is necessary to derivatize MSIA tips based on the analyte of interest. The main use of these tips are to flow samples through and the analytes affinity for the bound antigen/antibody allows for the capture of analyte. Non specifically bound compounds are rinsed out of the MSIA tips.
  The process can be simplified into 6 simple steps which Thermo termed the "work flow".
  #Gather Sample
  #Load Affinity Ligand
  #Purify Target Analyte
  #Elute Target Analyte
  #Pre-MS Sampling Process
  #MS Analysis
  Many "work flows" are commercially available for purchase.